3WCW
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound form
Summary for 3WCW
Entry DOI | 10.2210/pdb3wcw/pdb |
Related | 3WCT 3WCU 3WCV |
Descriptor | A1 globin chain of giant V2 hemoglobin, A2 globin chain of giant V2 hemoglobin, B2 globin chain of giant V2 hemoglobin, ... (9 entities in total) |
Functional Keywords | globin fold, oxygen transport, oxygen binding, blood |
Biological source | Lamellibrachia satsuma (Hydrothermal vent tubeworm) More |
Total number of polymer chains | 8 |
Total formula weight | 137512.30 |
Authors | Numoto, N.,Nakagawa, T.,Ohara, R.,Hasegawa, T.,Kita, A.,Yoshida, T.,Maruyama, T.,Imai, K.,Fukumori, Y.,Miki, K. (deposition date: 2013-06-01, release date: 2014-06-04, Last modification date: 2023-11-08) |
Primary citation | Numoto, N.,Nakagawa, T.,Ohara, R.,Hasegawa, T.,Kita, A.,Yoshida, T.,Maruyama, T.,Imai, K.,Fukumori, Y.,Miki, K. The structure of a deoxygenated 400 kDa haemoglobin reveals ternary- and quaternary-structural changes of giant haemoglobins Acta Crystallogr.,Sect.D, 70:1823-1831, 2014 Cited by PubMed: 25004960DOI: 10.1107/S1399004714008475 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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